Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production - Wikidata - wikimedia - TriplyDB

Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production

Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production

http://www.wikidata.org/entity/Q34391721

about

HIV-1 Vpu neutralizes the antiviral factor Tetherin/BST-2 by binding it and directing its beta-TrCP2-dependent degradation The formation of cysteine-linked dimers of BST-2/tetherin is important for inhibition of HIV-1 virus release but not for sensitivity to Vpu The cell biology of HIV-1 and other retroviruses Species-specific activity of SIV Nef and HIV-1 Vpu in overcoming restriction by tetherin/BST2 Regulated degradation of the HIV-1 Vpu protein through a betaTrCP-independent pathway limits the release of viral particles Broad-spectrum inhibition of retroviral and filoviral particle release by tetherin The restriction factors of human immunodeficiency virus How SAMHD1 changes our view of viral restriction HIV-1 Vpu targets cell surface markers CD4 and BST-2 through distinct mechanisms Vpu directs the degradation of the human immunodeficiency virus restriction factor BST-2/Tetherin via a {beta}TrCP-dependent mechanism HIV-1 accessory protein Vpu internalizes cell-surface BST-2/tetherin through transmembrane interactions leading to lysosomes Human immunodeficiency virus type 1 Vpu protein interacts with CD74 and modulates major histocompatibility complex class II presentation Intracellular immunity to HIV-1: newly defined retroviral battles inside infected cells.HIV Genome-Wide Protein Associations: a Review of 30 Years of Research The role of BST-2/Tetherin in host protection and disease manifestation Remodeling of the Host Cell Plasma Membrane by HIV-1 Nef and Vpu: A Strategy to Ensure Viral Fitness and Persistence HIV restriction in quiescent CD4⁺ T cells Direct restriction of virus release and incorporation of the interferon-induced protein BST-2 into HIV-1 particles Plasma membrane is the site of productive HIV-1 particle assembly Conformational changes induced by a single amino acid substitution in thetrans-membrane domain of Vpu: Implications for HIV-1 susceptibility to channel blocking drugs Structural and functional studies on the extracellular domain of BST2/tetherin in reduced and oxidized conformations Roles of HIV-1 auxiliary proteins in viral pathogenesis and host-pathogen interactions Immunoelectron microscopic evidence for Tetherin/BST2 as the physical bridge between HIV-1 virions and the plasma membrane Lv4 Is a Capsid-Specific Antiviral Activity in Human Blood Cells That Restricts Viruses of the SIVMAC/SIVSM/HIV-2 Lineage Prior to Integration Vpu and BST2: Still Not There Yet?The interferon-induced protein BST-2 restricts HIV-1 release and is downregulated from the cell surface by the viral Vpu protein Modulation of HIV-1-host interaction: role of the Vpu accessory protein Sequence of human immunodeficiency virus type 1 (HIV-1) Gag localization and oligomerization monitored with live confocal imaging of a replication-competent, fluorescently tagged HIV-1.HIV-1 Vpu promotes release and prevents endocytosis of nascent retrovirus particles from the plasma membrane.Demonstration of a novel HIV-1 restriction phenotype from a human T cell line Species-specific activity of HIV-1 Vpu and positive selection of tetherin transmembrane domain variants CAML does not modulate tetherin-mediated restriction of HIV-1 particle release Antagonism of tetherin restriction of HIV-1 release by Vpu involves binding and sequestration of the restriction factor in a perinuclear compartment Novel approaches to inhibiting HIV-1 replication.Functional domains within the human immunodeficiency virus type 2 envelope protein required to enhance virus production.Antiviral activity of the interferon-induced cellular protein BST-2/tetherin.Completion of hepatitis C virus replication cycle in heterokaryons excludes dominant restrictions in human non-liver and mouse liver cell lines.Polarity changes in the transmembrane domain core of HIV-1 Vpu inhibits its anti-tetherin activity.Viral replication is enhanced by an HIV-1 intersubtype recombination-derived Vpu protein.Cell-cell spread of human immunodeficiency virus type 1 overcomes tetherin/BST-2-mediated restriction in T cells.

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Viral protein U counteracts a human host cell restriction that inhibits HIV-1 particle production

http://www.wikidata.org/entity/Q34391721

description

2003 nî lūn-bûn

@nan

2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

@zh-hant

2003年論文

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2003年論文

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2003年論文

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2003年论文

@wuu

name

Viral protein U counteracts a ...... bits HIV-1 particle production

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Proceedings of the National Academy of Sciences of the United States of America

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Viral protein U counteracts a ...... bits HIV-1 particle production

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P2093

Klaus Strebel

http://www.w3.org/2001/XMLSchema#string

Paul Spearman

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Rita M Smith

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Vasundhara Varthakavi

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P2860

Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding

Vpu protein of human immunodeficiency virus type 1 enhances the release of capsids produced by gag gene constructs of widely divergent retroviruses

Differential activities of the human immunodeficiency virus type 1-encoded Vpu protein are regulated by phosphorylation and occur in different cellular compartments

The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation

Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein

Cell type-dependence for Vpu function

A novel human WD protein, h-beta TrCp, that interacts with HIV-1 Vpu connects CD4 to the ER degradation pathway through an F-box motif

Evidence for a newly discovered cellular anti-HIV-1 phenotype

A binding pocket for a small molecule inhibitor of HIV-1 entry within the transmembrane helices of CCR5

SCH-C (SCH 351125), an orally bioavailable, small molecule antagonist of the chemokine receptor CCR5, is a potent inhibitor of HIV-1 infection in vitro and in vivo

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100

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8975330

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14657387

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299932

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